Protein profile

KP13_04579

Catalase-peroxidase bifunctional enzyme

Genome: KpKP13

Gene: AHE44454.1 katG Structure source: AlphaFold + ColabFold UniProt A0A0H3GQ65

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Amino acids 725

Annotations 9

Features 45

PDB binders 6

Druggability 0.988

Overview

Basic information about this protein and its source genome.

Accession: KP13_04579
Assembly: Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene: AHE44454.1 katG
Status: annotated
Amino acids: 725
Structure source: AlphaFold + ColabFold

1.11.1.21

GO:0004096 Catalysis of the reaction: 2 H2O2 = O2 + 2 H2O. GO:0020037 Binding to a heme, a compound composed of iron complexed in a porphyrin (tetrapyrrole) ring. GO:0004601 Catalysis of the reaction: a reduced substrate + ROOH = an oxidized substrate + ROH + H2O. GO:0006979 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of oxidative stress, a state often resulting from exposure to high levels of reactive oxygen species, e.g. superoxide anions, hydrogen peroxide (H2O2), and hydroxyl radicals. GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. GO:0046872 Binding to a metal ion.

Target profile

Computed evidence for target prioritization.

Human off-target: No hit
Human identity (%): 0.0
Gut microbiome off-target: hit
Essential (DEG): Y
DEG identity (%): 82.759
DEG E-value: 0.0
Localization: Cytoplasmic
ColabFold pLDDT: 95.11

Selected Druggability evidence

AlphaFold / UniProt model

Selected Druggability is the FPocket score chosen for ranking using the curated structure priority. The 3D viewer may show a different loaded structure, so its visible pockets can differ.

FPocket 0.988

Structure A0A0H3GQ65

Pocket Pocket 2

P2Rank 0.985

Structure A0A0H3GQ65

Pocket Pocket 1

ColabFold model

FPocket 0.96 · Pocket 1

P2Rank 0.985 · Pocket 1

Core conservation Accessory gene

Roary accessory

CoreCruncher accessory

Gut microbiome 128 / 4744 genomes with a hit

Normalized 0.027

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 8 GO

Enzyme Commission (EC)

1.11.1.21

Gene Ontology (GO)

GO:0004096 Catalysis of the reaction: 2 H2O2 = O2 + 2 H2O.
GO:0020037 Binding to a heme, a compound composed of iron complexed in a porphyrin (tetrapyrrole) ring.
GO:0004601 Catalysis of the reaction: a reduced substrate + ROOH = an oxidized substrate + ROH + H2O.
GO:0006979 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of oxidative stress, a state often resulting from exposure to high levels of reactive oxygen species, e.g. superoxide anions, hydrogen peroxide (H2O2), and hydroxyl radicals.
GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
GO:0046872 Binding to a metal ion.
GO:0070301 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a hydrogen peroxide (H2O2) stimulus.
GO:0042744 The chemical reactions and pathways resulting in the breakdown of hydrogen peroxide (H2O2).

Sequence Features

Domain/signature hits from InterPro and related databases.

45 records

Show feature table

Start	End	DB	Term	Name
198	395	Gene3D	G3DSA:1.10.420.10	Peroxidase, domain 2
59	72	PRINTS	PR00460	Bacterial haem catalase-peroxidase signature
59	72	InterPro	IPR000763	Catalase-peroxidase haem
479	505	PRINTS	PR00460	Bacterial haem catalase-peroxidase signature
479	505	InterPro	IPR000763	Catalase-peroxidase haem
267	290	PRINTS	PR00460	Bacterial haem catalase-peroxidase signature
267	290	InterPro	IPR000763	Catalase-peroxidase haem
74	99	PRINTS	PR00460	Bacterial haem catalase-peroxidase signature
74	99	InterPro	IPR000763	Catalase-peroxidase haem
33	55	PRINTS	PR00460	Bacterial haem catalase-peroxidase signature
33	55	InterPro	IPR000763	Catalase-peroxidase haem
198	395	FunFam	G3DSA:1.10.420.10:FF:000002	Catalase-peroxidase
318	333	PRINTS	PR00458	Haem peroxidase superfamily signature
318	333	InterPro	IPR002016	Haem peroxidase
175	187	PRINTS	PR00458	Haem peroxidase superfamily signature
175	187	InterPro	IPR002016	Haem peroxidase
157	174	PRINTS	PR00458	Haem peroxidase superfamily signature
157	174	InterPro	IPR002016	Haem peroxidase
259	274	PRINTS	PR00458	Haem peroxidase superfamily signature
259	274	InterPro	IPR002016	Haem peroxidase
97	111	PRINTS	PR00458	Haem peroxidase superfamily signature
97	111	InterPro	IPR002016	Haem peroxidase
11	725	Hamap	MF_01961	Catalase-peroxidase [katG].
11	725	InterPro	IPR000763	Catalase-peroxidase haem
33	221	FunFam	G3DSA:1.10.520.10:FF:000002	Catalase-peroxidase
1	33	MobiDBLite	mobidb-lite	consensus disorder prediction
24	725	NCBIfam	TIGR00198	catalase/peroxidase HPI
24	725	InterPro	IPR000763	Catalase-peroxidase haem
435	725	SUPERFAMILY	SSF48113	Heme-dependent peroxidases
435	725	InterPro	IPR010255	Haem peroxidase superfamily
139	424	ProSiteProfiles	PS50873	Plant heme peroxidase family profile.
139	424	InterPro	IPR002016	Haem peroxidase
578	701	FunFam	G3DSA:1.10.420.10:FF:000004	Catalase-peroxidase
1	725	PANTHER	PTHR30555	HYDROPEROXIDASE I, BIFUNCTIONAL CATALASE-PEROXIDASE
1	725	InterPro	IPR000763	Catalase-peroxidase haem
436	722	CDD	cd08200	catalase_peroxidase_2
574	701	Gene3D	G3DSA:1.10.420.10	Peroxidase, domain 2
403	698	Pfam	PF00141	Peroxidase
403	698	InterPro	IPR002016	Haem peroxidase
83	396	Pfam	PF00141	Peroxidase
83	396	InterPro	IPR002016	Haem peroxidase
32	430	Gene3D	G3DSA:1.10.520.10	-
29	429	SUPERFAMILY	SSF48113	Heme-dependent peroxidases
29	429	InterPro	IPR010255	Haem peroxidase superfamily
435	725	Gene3D	G3DSA:1.10.520.10	-

3D Structure

Selected loaded structure. Experimental PDB entries may cover only a portion of the sequence; predicted models typically cover the full protein.

Loading 3D structure...

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Structural evidence

0 + 2

Experimental PDB entries and predicted models. Click Switch to display a different structure in the viewer.

Entry	Method	Resolution	Chain	Coverage	Links	Status
AlphaFold AF_A0A0H3GQ65	AlphaFold	—	—	full sequence	—	Viewing
ColabFold KP13_04579	ColabFold	—	—	full sequence	—	Loaded

Pocket details FPocket · P2Rank — toggle visibility and zoom from here, or open full viewer

Pockets (FPOCKET)

Showing top-ranked FPocket candidates by druggability. Druggability is color-coded: high (0.7 or higher), medium (0.4 to 0.69), low (below 0.4).

FPOCKET	Sticks	Spheres	Surfaces	Druggability	Labels	Zoom	Positions
2				0.988

Pockets (P2RANK)

Showing top-ranked P2Rank candidates by probability. Probability is color-coded per P2Rank calibration: high (≥ 0.5), medium (0.2 – 0.49), low (< 0.2).

P2RANK	Score	Probability
1	40.84	0.964
2	3.32	0.117
3	3.11	0.105
4	2.4	0.064
5	2.31	0.059

Pockets (FPOCKET)

Showing top-ranked FPocket candidates by druggability. Druggability is color-coded: high (0.7 or higher), medium (0.4 to 0.69), low (below 0.4).

FPOCKET	Sticks	Spheres	Surfaces	Druggability	Labels	Zoom	Positions
1				0.96

Pockets (P2RANK)

Showing top-ranked P2Rank candidates by probability. Probability is color-coded per P2Rank calibration: high (≥ 0.5), medium (0.2 – 0.49), low (< 0.2).

P2RANK	Score	Probability
1	38.84	0.961
2	2.97	0.096
3	2.54	0.071
4	1.92	0.039
5	1.56	0.024

Ligand evidence

Ligands grouped by evidence source. PDB ligands keep the source crystal visible, and loaded crystals can be opened directly in the structure viewer.

56 records

Highest-confidence structural evidence: ligands co-crystallized with this exact protein. If the source PDB is loaded in TPW, use Open crystal to inspect it in the structure viewer.

No PDB structure with a co-crystallized ligand found for this exact protein.

Structural evidence inferred from similar proteins. The source crystal indicates where the ligand was observed; the UniProt column identifies the homologous protein carrying that ligand.

Ligand	Source crystal	UniProt (homolog)	MW · LogP · TPSA	Lipinski	PAINS	SMILES
DDJ	3VLJ	O59651	244.3 Da LogP 2.54 TPSA 70.5	✓ Ro5	✓ Clean	`COc1cc(ccc1N)c2ccc(c(c2)OC)N`
FLC	5JHX	A4QUT2	189.1 Da LogP -5.25 TPSA 140.6	✓ Ro5	✓ Clean	`C(C(=O)[O-])C(CC(=O)[O-])(C(=O)[O-])O`
NIZ	3WXO	Q31MN3	137.1 Da LogP -0.31 TPSA 68.0	✓ Ro5	✓ Clean	`c1cnccc1C(=O)NN`
O	5SW6	Q3JNW6	18.0 Da LogP -0.82 TPSA 31.5	✓ Ro5	✓ Clean	`O`
OXY	5KQ6	Q3JNW6	32.0 Da LogP 0.07 TPSA 34.1	✓ Ro5	✓ Clean	`O=O`
SHA	3VLL	O59651	153.1 Da LogP 0.51 TPSA 69.6	✓ Ro5	✓ Clean	`c1ccc(c(c1)C(=O)NO)O`

Experimental bioactivity from ChEMBL measured directly on this protein. Score = pchembl (−log Ki/IC₅₀; higher = more potent).

No ChEMBL bioactivity data found for this exact protein.

Bioactivity inferred from similar proteins in ChEMBL. Score = pchembl (−log Ki/IC₅₀; higher = more potent).

No ChEMBL hits found through similar proteins.

Proposed virtual-screening candidates from ZINC. Score = Tanimoto similarity to a known binder (0–1; higher = more similar).

Ligand	Tanimoto	MW · LogP · TPSA	Lipinski	PAINS	SMILES
ZINC56395	1.000	244.3 Da LogP 2.54 TPSA 70.5	✓ Ro5	✓ Clean	`COc1cc(-c2ccc(N)c(OC)c2)ccc1N`
ZINC83315	1.000	204.2 Da LogP 1.12 TPSA 79.1	✓ Ro5	✓ Clean	`N[C@@H](Cc1c[nH]c2ccccc12)C(=O)O`
ZINC83317	1.000	204.2 Da LogP 1.12 TPSA 79.1	✓ Ro5	✓ Clean	`N[C@H](Cc1c[nH]c2ccccc12)C(=O)O`
ZINC403598	0.800	273.3 Da LogP 2.14 TPSA 92.8	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc(Oc2ccc(O)cc2)cc1)C(=O)O`
ZINC403599	0.800	273.3 Da LogP 2.14 TPSA 92.8	✓ Ro5	✓ Clean	`N[C@H](Cc1ccc(Oc2ccc(O)cc2)cc1)C(=O)O`
ZINC4899521	0.778	203.2 Da LogP 0.52 TPSA 84.9	✓ Ro5	✓ Clean	`NC(=O)[C@H](N)Cc1c[nH]c2ccccc12`
ZINC57505	0.778	203.2 Da LogP 0.52 TPSA 84.9	✓ Ro5	✓ Clean	`NC(=O)[C@@H](N)Cc1c[nH]c2ccccc12`
ZINC2566035	0.757	218.3 Da LogP 1.51 TPSA 79.1	✓ Ro5	✓ Clean	`N[C@@H](CCc1c[nH]c2ccccc12)C(=O)O`
ZINC6864822	0.757	218.3 Da LogP 1.51 TPSA 79.1	✓ Ro5	✓ Clean	`N[C@H](CCc1c[nH]c2ccccc12)C(=O)O`
ZINC1690614	0.743	233.2 Da LogP 1.50 TPSA 90.4	✓ Ro5	✓ Clean	`O=C(O)C(Cc1c[nH]c2ccccc12)C(=O)O`
ZINC39351856	0.741	328.4 Da LogP 1.26 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc(-c2ccc(C[C@H](N)C(=O)O)cc2)cc1)C…`
ZINC1637998	0.732	261.3 Da LogP 0.24 TPSA 108.2	✓ Ro5	✓ Clean	`N[C@H](Cc1c[nH]c2ccccc12)C(=O)NCC(=O)O`
ZINC2384992	0.732	261.3 Da LogP 0.24 TPSA 108.2	✓ Ro5	✓ Clean	`N[C@@H](Cc1c[nH]c2ccccc12)C(=O)NCC(=O)O`
ZINC264238	0.732	293.4 Da LogP 2.35 TPSA 70.9	✓ Ro5	✓ Clean	`N[C@H](Cc1c[nH]c2ccccc12)C(=O)NCc1ccccc1`
ZINC264242	0.732	293.4 Da LogP 2.35 TPSA 70.9	✓ Ro5	✓ Clean	`N[C@@H](Cc1c[nH]c2ccccc12)C(=O)NCc1ccccc1`
ZINC34781219	0.718	218.3 Da LogP 1.21 TPSA 68.1	✓ Ro5	✓ Clean	`COC(=O)[C@H](N)Cc1c[nH]c2ccccc12`
ZINC34781220	0.718	218.3 Da LogP 1.21 TPSA 68.1	✓ Ro5	✓ Clean	`COC(=O)[C@@H](N)Cc1c[nH]c2ccccc12`
ZINC1557161	0.714	390.4 Da LogP 2.33 TPSA 124.0	✓ Ro5	✓ Clean	`N[C@@H](Cc1c[nH]c2ccccc12)C(=O)N[C@@H](Cc1c[nH]…`
ZINC1557164	0.714	390.4 Da LogP 2.33 TPSA 124.0	✓ Ro5	✓ Clean	`N[C@H](Cc1c[nH]c2ccccc12)C(=O)N[C@H](Cc1c[nH]c2…`
ZINC193616	0.707	279.3 Da LogP 2.68 TPSA 70.9	✓ Ro5	✓ Clean	`N[C@H](Cc1c[nH]c2ccccc12)C(=O)Nc1ccccc1`
ZINC2497690	0.707	279.3 Da LogP 2.68 TPSA 70.9	✓ Ro5	✓ Clean	`N[C@@H](Cc1c[nH]c2ccccc12)C(=O)Nc1ccccc1`
ZINC874230	0.707	231.3 Da LogP 1.17 TPSA 70.9	✓ Ro5	✓ Clean	`CCNC(=O)[C@H](N)Cc1c[nH]c2ccccc12`
ZINC874233	0.707	231.3 Da LogP 1.17 TPSA 70.9	✓ Ro5	✓ Clean	`CCNC(=O)[C@@H](N)Cc1c[nH]c2ccccc12`
ZINC39098	0.703	205.2 Da LogP 1.16 TPSA 73.3	✓ Ro5	✓ Clean	`O=C(O)[C@@H](O)Cc1c[nH]c2ccccc12`
ZINC39099	0.703	205.2 Da LogP 1.16 TPSA 73.3	✓ Ro5	✓ Clean	`O=C(O)[C@H](O)Cc1c[nH]c2ccccc12`
ZINC83138991	0.703	268.1 Da LogP 2.56 TPSA 53.1	✓ Ro5	✓ Clean	`O=C(O)[C@@H](Br)Cc1c[nH]c2ccccc12`
ZINC34307123	0.700	217.3 Da LogP 0.78 TPSA 70.9	✓ Ro5	✓ Clean	`CNC(=O)[C@@H](N)Cc1c[nH]c2ccccc12`
ZINC34482181	0.700	217.3 Da LogP 0.78 TPSA 70.9	✓ Ro5	✓ Clean	`CNC(=O)[C@H](N)Cc1c[nH]c2ccccc12`
ZINC52968847	0.700	232.3 Da LogP 1.60 TPSA 68.1	✓ Ro5	✓ Clean	`CCOC(=O)[C@@H](N)Cc1c[nH]c2ccccc12`
ZINC53943847	0.700	232.3 Da LogP 1.60 TPSA 68.1	✓ Ro5	✓ Clean	`CCOC(=O)[C@H](N)Cc1c[nH]c2ccccc12`
ZINC1638007	0.698	275.3 Da LogP 0.63 TPSA 108.2	✓ Ro5	✓ Clean	`C[C@H](NC(=O)[C@@H](N)Cc1c[nH]c2ccccc12)C(=O)O`
ZINC2453187	0.696	257.2 Da LogP 1.67 TPSA 86.6	✓ Ro5	✓ Clean	`O=C(NC(=O)c1ccccc1O)c1ccccc1O`
ZINC4240327	0.692	218.3 Da LogP 1.51 TPSA 79.1	✓ Ro5	✓ Clean	`N[C@H](CC(=O)O)Cc1c[nH]c2ccccc12`
ZINC44544883	0.692	218.3 Da LogP 1.37 TPSA 79.1	✓ Ro5	✓ Clean	`NC[C@H](Cc1c[nH]c2ccccc12)C(=O)O`
ZINC44544886	0.692	218.3 Da LogP 1.37 TPSA 79.1	✓ Ro5	✓ Clean	`NC[C@@H](Cc1c[nH]c2ccccc12)C(=O)O`
ZINC4521117	0.692	218.3 Da LogP 1.51 TPSA 79.1	✓ Ro5	✓ Clean	`N[C@@H](CC(=O)O)Cc1c[nH]c2ccccc12`
ZINC2134508	0.690	245.3 Da LogP 1.56 TPSA 70.9	✓ Ro5	✓ Clean	`CCCNC(=O)[C@H](N)Cc1c[nH]c2ccccc12`
ZINC2134510	0.690	245.3 Da LogP 1.56 TPSA 70.9	✓ Ro5	✓ Clean	`CCCNC(=O)[C@@H](N)Cc1c[nH]c2ccccc12`
ZINC2559489	0.690	260.3 Da LogP -0.36 TPSA 114.0	✓ Ro5	✓ Clean	`NC(=O)CNC(=O)[C@@H](N)Cc1c[nH]c2ccccc12`
ZINC32333	0.690	244.1 Da LogP 1.40 TPSA 63.3	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc(Br)cc1)C(=O)O`
ZINC32334	0.690	244.1 Da LogP 1.40 TPSA 63.3	✓ Ro5	✓ Clean	`N[C@H](Cc1ccc(Br)cc1)C(=O)O`
ZINC3679925	0.690	291.1 Da LogP 1.25 TPSA 63.3	✓ Ro5	✓ Clean	`N[C@H](Cc1ccc(I)cc1)C(=O)O`
ZINC391104	0.690	291.1 Da LogP 1.25 TPSA 63.3	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc(I)cc1)C(=O)O`
ZINC4202286	0.690	209.2 Da LogP 0.34 TPSA 100.6	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc(C(=O)O)cc1)C(=O)O`
ZINC4202287	0.690	209.2 Da LogP 0.34 TPSA 100.6	✓ Ro5	✓ Clean	`N[C@H](Cc1ccc(C(=O)O)cc1)C(=O)O`
ZINC6092920	0.690	223.2 Da LogP 0.27 TPSA 100.6	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc(CC(=O)O)cc1)C(=O)O`
ZINC6506146	0.690	223.2 Da LogP 0.27 TPSA 100.6	✓ Ro5	✓ Clean	`N[C@H](Cc1ccc(CC(=O)O)cc1)C(=O)O`
ZINC34319489	0.688	231.3 Da LogP 1.50 TPSA 83.5	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc2cc(O)ccc2c1)C(=O)O`
ZINC34319490	0.688	231.3 Da LogP 1.50 TPSA 83.5	✓ Ro5	✓ Clean	`N[C@H](Cc1ccc2cc(O)ccc2c1)C(=O)O`
ZINC178387	0.684	203.2 Da LogP 2.43 TPSA 53.1	✓ Ro5	✓ Clean	`C[C@H](Cc1c[nH]c2ccccc12)C(=O)O`

PDB and ChEMBL records on this protein are shown in full. ChEMBL records from similar proteins are capped at the top 100 per protein (by pchembl) and ZINC at the top 50 (Tanimoto ≥ 0.5). ADME columns are descriptor-based screening flags, not experimental toxicity results.